SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Synpcc7942_0485 FitnessBrowser__SynE:Synpcc7942_0485 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
34% identity, 46% coverage: 229:432/445 of query aligns to 2:200/207 of 4ij6A

query
sites
4ij6A

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active site: R8 (= R235), A9 (≠ H236), N15 (= N242), R58 (= R285), E82 (= E310), H150 (= H379)
binding phosphoserine: R8 (= R235), Q21 (= Q248), R58 (= R285), E82 (= E310), H85 (= H313), H150 (= H379), T151 (≠ D380)

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
27% identity, 44% coverage: 3:200/445 of query aligns to 2:183/196 of 6m1xC

query
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6m1xC

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binding 3-phosphoglyceric acid: R8 (= R9), H9 (= H10), Q21 (= Q22), R57 (= R60), E79 (= E86), H146 (= H163), G147 (≠ N164)

Q9NQ88 Fructose-2,6-bisphosphatase TIGAR; TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; EC 3.1.3.46 from Homo sapiens (Human) (see 4 papers)
26% identity, 47% coverage: 231:439/445 of query aligns to 6:270/270 of Q9NQ88

query
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Q9NQ88

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H11 (= H236) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.
E102 (= E323) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.
H198 (= H379) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.
NLQD 258:261 (≠ NLTL 427:430) mutation Missing: Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.

5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
27% identity, 44% coverage: 3:200/445 of query aligns to 2:183/198 of 5zr2C

query
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5zr2C

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binding phosphoserine: R8 (= R9), Q21 (= Q22), G22 (= G23), R57 (= R60), E79 (= E86), H146 (= H163), G147 (≠ N164)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
32% identity, 41% coverage: 231:412/445 of query aligns to 4:184/207 of 1h2fA

query
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1h2fA

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active site: R8 (= R235), H9 (= H236), N15 (= N242), R58 (= R285), E82 (= E310), H150 (= H379)
binding phosphate ion: G142 (= G371), E143 (≠ S372)
binding trivanadate: R8 (= R235), H9 (= H236), N15 (= N242), Q21 (= Q248), R58 (= R285), E82 (= E310), H150 (= H379), G151 (≠ D380), V152 (≠ A381)

Sites not aligning to the query:

binding phosphate ion: 1, 2, 3

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
32% identity, 41% coverage: 231:412/445 of query aligns to 4:184/207 of 1h2eA

query
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1h2eA

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E

E

L

-

I

I

L

V

E

R

R

G

H

G

P

R

N

L

C

I

E

P

L

I

S

Y

V

Q

D

D

D

E

R

R

L

L

Q

R

E
|
E

I

I

G

H

H

L

G

G

L

D

W

W

E

E

G

G

K

K

L

T

E

H

E

D

E

E

I

I

A

R

A

Q

E

M

F

D

G

P

E

I

L

A

L

F

Q

D

L

H

W

F

K

W

D

Q

Q

A

P

P

E

H

Q

L

V

Y

Q

A

M

P

P

Q

E

R

G

G

E

E

N

R

L

F

Q

C

E

D

V

V

W

Q

D

Q

R

R

S

A

V

L

A

E

A

A

W

V

E

Q

A

S

I

I

V

V

A

-

N

D

A

R

P

H

E

E

G

G

S

E

T

T

G

V

L

L

V

I

V

V

A

T

H
|
H

D

G

A

V

V

V

N

L

K

K

V

T

I

L

L

M

C

A

H

A

V

F

L

K

G

D

L

T

S

P

P

L

A

D

D

H

I

L

W

W

S

S

I

P

K

P

Q

Y

G

M

N

Y

G

G

-

T

A

S

V

V

T

T

V

I

D

E

active site: R8 (= R235), H9 (= H236), N15 (= N242), R58 (= R285), E82 (= E310), H150 (= H379)
binding phosphate ion: R8 (= R235), H9 (= H236), R58 (= R285), E82 (= E310), H150 (= H379)

2h4zA Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate (see paper)
28% identity, 43% coverage: 227:417/445 of query aligns to 1:225/255 of 2h4zA

query
sites
2h4zA

S

S

G

K

V

Y

R

K

L

L

L

I

L

M

V

L

R
|
R

H
|
H

G

G

E

E

T

G

D

A

W

W

N

N

R

K

Q

E

K

N

R

R

F

F

Q
x
C

G
x
S

Q

W

I

V

D

D

I

Q

P

K

L

L

N

N

D

S

N

E

G

G

R

M

A

E

Q

E

A

A

R

R

S

N

A

C

A

G

E

K

F

Q

L

L

A

K

P

A

I

L

Q

N

I

F

D

E

F

F

-

D

-

L

A

V

V

F

S

T

S

S

P

V

M

L

A

N

R
|
R

P

S

K

I

E

H

T

T

A

A

E

W

L

L

I

I

L

L

E

E

R

E

H

L

P

G

N

Q

C

E

E

W

L

V

S

P

V

V

D

E

D

S

-

S

-

W

R

R

L

L

Q

N

E
|
E

I

R

G

H

H
x
Y

G

G

L

A

W

L

E

I

G

G

K

L

L

N

E
x
R

E

E

E

Q

I

M

A

A

A

L

E

N

F

H

G

G

-

E

E

E

L

Q

L

V

Q

R

L

L

W

W

K
x
R

-
x
R

-

S

-

Y

-

N

-

V

-

T

-

P

-

I

-

E

-

S

-

H

-

P

-

Y

-

Q

-

E

-

I

-

Y

-

N

D

D

Q

R

P

R

E

Y

Q

K

V

V

-

C

-

D

-

V

-

P

-

L

-

D

Q

Q

M

L

P

P

E

R

G

S

E

E

N

S

L

L

Q

K

E

D

V

V

W

L

D

E

R

R

S

L

V

L

A

P

A

Y

W

W

-

N

E

E

A

R

I

I

V

A

A

P

N

E

A

V

P

L

E

R

G

G

S

K

T

T

G

I

L

L

V

I

V

S

A

A

H
|
H

D

G

A
x
N

V

S

N

S

K

R

V

A

I

L

L

L

C

K

H

H

V

L

L

E

G

G

L

I

S

S

P

D

A

E

D

D

I

I

W

I

S

N

I

I

K

T

Q

L

G

P

N

T

G

G

A

V

V

P

T

I

V

L

D

E

Y

L

P

D

K

E

R

N

L

L

active site: H10 (= H236), R61 (= R285), E88 (= E310), H187 (= H379)
binding (2R)-2,3-diphosphoglyceric acid: R9 (= R235), H10 (= H236), C22 (≠ Q248), S23 (≠ G249), R61 (= R285), E88 (= E310), Y91 (≠ H313), R99 (≠ E321), R115 (≠ K336), R116 (vs. gap), H187 (= H379), N189 (≠ A381)

P07738 Bisphosphoglycerate mutase; BPGM; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; 2,3-diphosphoglycerate mutase; DPGM; BPG-dependent PGAM; EC 5.4.2.4; EC 5.4.2.11 from Homo sapiens (Human) (see 5 papers)
28% identity, 43% coverage: 227:417/445 of query aligns to 2:226/259 of P07738

query
sites
P07738

S

S

G
x
K

V

Y

R
x
K

L

L

L

I

L

M

V

L

R
|
R

H
|
H

G
|
G

E
|
E

T
x
G

D
x
A

W
|
W

N
|
N

R
x
K

Q

E

K

N

R

R

F

F

Q
x
C

G
x
S

Q

W

I

V

D

D

I

Q

P
x
K

L

L

N

N

D

S

N

E

G

G

R

M

A

E

Q

E

A

A

R

R

S

N

A

C

A

G

E
x
K

F

Q

L

L

A
x
K

P

A

I

L

Q

N

I

F

D

E

F

F

-

D

-

L

A

V

V

F

S

T

S

S

P

V

M

L

A

N

R
|
R

P

S

K

I

E

H

T

T

A

A

E

W

L

L

I

I

L

L

E

E

R

E

H

L

P

G

N

Q

C

E

E

W

L

V

S

P

V

V

D

E

D

S

-

S

-

W

R

R

L

L

Q

N

E
|
E

I
x
R

G
x
H

H
x
Y

G

G

L

A

W

L

E

I

G

G

K

L

L

N

E
x
R

E

E

E

Q

I

M

A

A

A

L

E

N

F

H

G

G

-

E

E

E

L

Q

L

V

Q

R

L

L

W

W

K
x
R

-
x
R

-

S

-

Y

-

N

-

V

-

T

-

P

-

I

-

E

-

S

-

H

-

P

-

Y

-

Q

-

E

-

I

-

Y

-

N

D

D

Q

R

P

R

E

Y

Q
x
K

V

V

-

C

-

D

-

V

-

P

-

L

-

D

Q

Q

M

L

P

P

E

R

G

S

E

E

N

S

L

L

Q
x
K

E

D

V

V

W

L

D

E

R

R

S

L

V

L

A

P

A

Y

W

W

-

N

E

E

A

R

I

I

V

A

A

P

N

E

A

V

P

L

E

R

G

G

S
x
K

T

T

G

I

L

L

V

I

V

S

A

A

H
|
H

D
x
G

A
x
N

V

S

N

S

K

R

V

A

I

L

L

L

C
x
K

H

H

V

L

L

E

G

G

L

I

S

S

P

D

A

E

D

D

I

I

W

I

S

N

I

I

K

T

Q

L

G

P

N

T

G

G

A

V

V

P

T

I

V

L

D

E

Y

L

P

D

K

E

R

N

L

L

K3 (≠ G228) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
K5 (≠ R230) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
10:17 (vs. 235:242, 75% identical) binding
H11 (= H236) active site, Tele-phosphohistidine intermediate
K18 (≠ R243) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
CS 23:24 (≠ QG 248:249) binding
K29 (≠ P254) Not glycated
K43 (≠ E268) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
K46 (≠ A271) Not glycated
R62 (= R285) binding
E89 (= E310) active site, Proton donor/acceptor
ERHY 89:92 (≠ EIGH 310:313) binding
R90 (≠ I311) to C: in ECYT8; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity; dbSNP:rs121964925
R100 (≠ E321) binding
RR 116:117 (≠ K- 336) binding
K143 (≠ Q341) Not glycated
K159 (≠ Q351) modified: carbohydrate, N-linked (Glc) (glycation) lysine
K181 (≠ S372) Not glycated
H188 (= H379) Transition state stabilizer
GN 189:190 (≠ DA 380:381) binding
K197 (≠ C388) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
246 Not glycated
247 Not glycated
253 Not glycated
258 Not glycated
259 Not glycated

5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
27% identity, 43% coverage: 230:421/445 of query aligns to 2:224/234 of 5pgmE

query
sites
5pgmE

R

K

L

L

L

V

L

L

V

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

R

E

Q

K

K

N

R

L

F

F

Q

T

G

G

Q

W

I

V

D

D

I

V

P

K

L

L

N

S

D

A

N

K

G

G

R

Q

A

Q

Q

E

A

A

R

A

S

R

A

A

A

G

E

E

F

L

L

L

A

K

P

E

I

K

Q

K

I

V

-

Y

-

P

D

D

F

V

A

L

V

Y

S

T

S

S

P

K

M

L

A

S

R
|
R

P

A

K

I

E

Q

T

T

A

A

E

N

L

I

I

A

L

L

E

E

R

K

H

A

P

D

N

R

C

L

E

W

L

I

S

P

V

V

D

N

D

R

-

S

-

W

R

R

L

L

Q

N

E
|
E

I

R

G

H

H

Y

G

G

L

D

W

L

E

Q

G

G

K

K

L

D

E

K

E

A

E

E

I

T

A

L

A

K

E

K

F

F

G

G

E

E

-

E

-

K

-

F

-

N

-

T

-

Y

-

R

-

S

-

F

-

D

-

V

-

P

-

I

-

D

-

A

-

S

-

P

L

F

L

S

Q

Q

L

K

W

G

K

D

D

E

Q

R

P

Y

E

K

Q

Y

V

V

Q

D

-

P

-

N

-

V

M

L

P

P

E

E

G

T

E

E

N

S

L

L

Q

A

E

L

V

V

W

I

D

D

R

R

S

L

V

L

A

P

A

Y

W

W

E

Q

A

D

I

V

V

I

A

A

-

K

N

D

A

L

P

L

E

S

G

G

S

K

T

T

G

V

L

M

V

I

V

A

A

A

H
|
H

D

G

A

N

V

S

N

L

K

R

V

G

I

L

L

V

C

K

H

H

V

L

L

E

G

G

L

I

S

S

P

D

A

A

D

D

I

I

W

A

S

K

I

L

K

N

Q

I

G

P

N

T

G

G

A

I

V

P

T

L

V

V

V

F

D

E

Y

L

P

D

K

E

R

N

L

L

D

K

-

P

S

S

R

K

P

P

active site: H8 (= H236), R59 (= R285), E86 (= E310), H181 (= H379)

Sites not aligning to the query:

binding alanine: 231, 234

1bq4A Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate (see paper)
27% identity, 43% coverage: 230:421/445 of query aligns to 2:224/234 of 1bq4A

query
sites
1bq4A

R

K

L

L

L

V

L

L

V

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

R

E

Q

K

K

N

R

L

F

F

Q

T

G

G

Q

W

I

V

D

D

I

V

P

K

L

L

N

S

D

A

N

K

G

G

R

Q

A

Q

Q

E

A

A

R

A

S

R

A

A

A

G

E

E

F

L

L

L

A

K

P

E

I

K

Q

K

I

V

-

Y

-

P

D

D

F

V

A

L

V

Y

S

T

S

S

P

K

M

L

A

S

R
|
R

P

A

K

I

E

Q

T

T

A

A

E

N

L

I

I

A

L

L

E

E

R

K

H

A

P

D

N

R

C

L

E

W

L

I

S

P

V

V

D

N

D

R

-

S

-

W

R

R

L

L

Q

N

E
|
E

I

R

G

H

H
x
Y

G

G

L

D

W

L

E

Q

G

G

K

K

L

D

E

K

E

A

E

E

I

T

A

L

A

K

E

K

F

F

G

G

E

E

-

E

-

K

-

F

-

N

-

T

-

Y

-
x
R

-

S

-

F

-

D

-

V

-

P

-

I

-

D

-

A

-

S

-

P

L

F

L

S

Q

Q

L

K

W

G

K

D

D

E

Q

R

P

Y

E

K

Q

Y

V

V

Q

D

-

P

-

N

-

V

M

L

P

P

E

E

G

T

E

E

N

S

L

L

Q

A

E

L

V

V

W

I

D

D

R

R

S

L

V

L

A

P

A

Y

W

W

E

Q

A

D

I

V

V

I

A

A

-

K

N

D

A

L

P

L

E

S

G

G

S

K

T

T

G

V

L

M

V

I

V

A

A

A

H
|
H

D

G

A
x
N

V

S

N

L

K

R

V

G

I

L

L

V

C

K

H

H

V

L

L

E

G

G

L

I

S

S

P

D

A

A

D

D

I

I

W

A

S

K

I

L

K
x
N

Q

I

G

P

N

T

G

G

A

I

V

P

T

L

V

V

V

F

D

E

Y

L

P

D

K

E

R

N

L

L

D

K

-

P

S

S

R

K

P

P

active site: H8 (= H236), R59 (= R285), E86 (= E310), H181 (= H379)
binding benzene hexacarboxylic acid: Y89 (≠ H313), R113 (vs. gap), R114 (vs. gap), N183 (≠ A381), N204 (≠ K402)

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
27% identity, 43% coverage: 230:421/445 of query aligns to 2:224/240 of 1qhfA

query
sites
1qhfA

R

K

L

L

L

V

L

L

V

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

D

E

W

W

N
|
N

R

E

Q

K

K

N

R

L

F

F

Q
x
T

G

G

Q

W

I

V

D

D

I

V

P

K

L

L

N

S

D

A

N

K

G

G

R

Q

A

Q

Q

E

A

A

R

A

S

R

A

A

A

G

E

E

F

L

L

L

A

K

P

E

I

K

Q

K

I

V

-

Y

-

P

D

D

F

V

A

L

V

Y

S

T

S

S

P

K

M

L

A

S

R
|
R

P

A

K

I

E

Q

T

T

A

A

E

N

L

I

I

A

L

L

E

E

R

K

H

A

P

D

N

R

C

L

E

W

L

I

S

P

V

V

D

N

D

R

-

S

-

W

R

R

L

L

Q

N

E
|
E

I

R

G

H

H

Y

G

G

L

D

W

L

E

Q

G

G

K

K

L

D

E

K

E

A

E

E

I

T

A

L

A

K

E

K

F

F

G

G

E

E

-

E

-

K

-

F

-

N

-

T

-

Y

-

R

-

S

-

F

-

D

-

V

-

P

-

I

-

D

-

A

-

S

-

P

L

F

L

S

Q

Q

L

K

W

G

K

D

D

E

Q

R

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E

K

Q

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-

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-

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-

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|
H

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A

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N
x
T

G

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A

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L

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-

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S

S

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P

P

active site: H8 (= H236), R59 (= R285), E86 (= E310), H181 (= H379)
binding 3-phosphoglyceric acid: R7 (= R235), H8 (= H236), G9 (= G237), Q10 (≠ E238), S11 (≠ T239), N14 (= N242), T20 (≠ Q248), R59 (= R285), T207 (≠ N405)

P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 37% coverage: 231:394/445 of query aligns to 10:178/211 of P36623

query
sites
P36623

L

L

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x
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T37 (≠ N258) modified: Phosphothreonine
S62 (= S281) modified: Phosphoserine
Y96 (≠ H313) modified: Phosphotyrosine
S166 (≠ V382) modified: Phosphoserine

7n3rB The ternary complex of human bisphosphoglycerate mutase with 3- phosphoglycerate and 2-phosphoglycolate (see paper)
28% identity, 42% coverage: 230:417/445 of query aligns to 3:224/239 of 7n3rB

query
sites
7n3rB

R

K

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L

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binding 2-phosphoglycolic acid: C21 (≠ Q248), S22 (≠ G249), E87 (= E310)

2f90A Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and alf4- (see paper)
28% identity, 42% coverage: 230:417/445 of query aligns to 3:224/254 of 2f90A

query
sites
2f90A

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H

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x
G

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L

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L

L

active site: H9 (= H236), R60 (= R285), E87 (= E310), H186 (= H379)
binding tetrafluoroaluminate ion: R8 (= R235), H9 (= H236), R60 (= R285), E87 (= E310), H186 (= H379), G187 (≠ D380)

Q7ZVE3 Fructose-2,6-bisphosphatase TIGAR B; TP53-induced glycolysis and apoptosis regulator B; EC 3.1.3.46 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
36% identity, 28% coverage: 231:356/445 of query aligns to 6:131/257 of Q7ZVE3

query
sites
Q7ZVE3

L

L

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H

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N

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R

H11 (= H236) active site, Tele-phosphohistidine intermediate

P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
37% identity, 32% coverage: 230:370/445 of query aligns to 5:143/223 of P9WIC7

query
sites
P9WIC7

R

R

L

L

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L

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R

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H

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x
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E

R10 (= R235) mutation to A: Loss of phosphatase activity.
H11 (= H236) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N242) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ P272) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R285) mutation to A: Loss of phosphatase activity.

Sites not aligning to the query:

159 H→A: About 5% of wild-type phosphatase activity.
209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
37% identity, 32% coverage: 230:370/445 of query aligns to 4:142/217 of 4pzaB

query
sites
4pzaB

R

R

L

L

L

V

L

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V

L

R
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R

H
|
H

G

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D

D

W

Y

N

N

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E

active site: H10 (= H236), R59 (= R285), E83 (= E310)
binding phosphate ion: R9 (= R235), H10 (= H236), R59 (= R285), E83 (= E310)

Sites not aligning to the query:

binding phosphate ion: 158, 159

3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
27% identity, 41% coverage: 230:412/445 of query aligns to 3:215/230 of 3fdzA

query
sites
3fdzA

R

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L

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L

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H

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x
T

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A

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active site: H9 (= H236), R60 (= R285), E87 (= E310), H182 (= H379)
binding (2R)-2,3-diphosphoglyceric acid: R8 (= R235), H9 (= H236), N15 (= N242), T21 (≠ Q248), R60 (= R285), E87 (= E310), Y90 (≠ H313), K98 (≠ E321), R114 (≠ K336), R115 (vs. gap), H182 (= H379), G183 (≠ D380), N184 (≠ A381)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
37% identity, 32% coverage: 230:370/445 of query aligns to 3:141/209 of 4qihA

query
sites
4qihA

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active site: H9 (= H236), R58 (= R285), E82 (= E310)
binding vanadate ion: R8 (= R235), H9 (= H236), Q21 (= Q248), R58 (= R285)

Sites not aligning to the query:

binding vanadate ion: 157

3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
27% identity, 41% coverage: 230:412/445 of query aligns to 3:215/229 of 3gp3A

query
sites
3gp3A

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active site: H9 (= H236), R60 (= R285), E87 (= E310), H182 (= H379)
binding phosphite ion: R8 (= R235), H9 (= H236), R60 (= R285), E87 (= E310), H182 (= H379), G183 (≠ D380)
binding phosphoserine: T21 (≠ Q248), E87 (= E310), Y90 (≠ H313), K98 (≠ E321), R114 (≠ K336), R115 (vs. gap), N184 (≠ A381)

Query Sequence

>Synpcc7942_0485 FitnessBrowser__SynE:Synpcc7942_0485
LATRVVLVRHGQSSYNAAGRIQGRCDNSQLTDRGAADAVKVAAALNGIPFAAAYCSPLQR
AKRTAEIIIEQIETPPALAVSDGLLEVDLPLWEGLSREEVRSQYAELYRQWHEAPHELVL
TVPDGQGGSREHAPVLALFEQARQFWKDLLERHRDQTVLLVAHNGILRSLIATALGVDPS
AYQVIRQSNCGISVLNFADGTNQPAQLECLNLTAPLGDALPDRGASSGVRLLLVRHGETD
WNRQKRFQGQIDIPLNDNGRAQARSAAEFLAPIQIDFAVSSPMARPKETAELILERHPNC
ELSVDDRLQEIGHGLWEGKLEEEIAAEFGELLQLWKDQPEQVQMPEGENLQEVWDRSVAA
WEAIVANAPEGSTGLVVAHDAVNKVILCHVLGLSPADIWSIKQGNGAVTVVDYPKRLDSR
PVLQAMNLTLHLDGAVLDRTAAGAL

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory